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Author Notes:

dreines@emory.edu

Conceptualization: Travis J. Loya, Joshua B. Kelley, Daniel Reines.

Data curation: Travis J. Loya, Thomas W. O’Rourke, William C. Simke, Joshua B. Kelley, Daniel Reines.

Formal analysis: Travis J. Loya, Thomas W. O’Rourke, Joshua B. Kelley, Daniel Reines.

Funding acquisition: Joshua B. Kelley, Daniel Reines.

Investigation: Travis J. Loya, Thomas W. O’Rourke, William C. Simke, Joshua B. Kelley, Daniel Reines.

Methodology: Travis J. Loya, William C. Simke, Joshua B. Kelley, Daniel Reines.

Project administration: Daniel Reines.

Resources: Daniel Reines.

Software: William C. Simke, Joshua B. Kelley.

Supervision: Joshua B. Kelley, Daniel Reines.

Validation: Travis J. Loya, Thomas W. O’Rourke, William C. Simke, Joshua B. Kelley, Daniel Reines.

Visualization: Travis J. Loya, Thomas W. O’Rourke, William C. Simke, Joshua B. Kelley, Daniel Reines.

Writing – original draft: Travis J. Loya, Thomas W. O’Rourke, William C. Simke, Joshua B. Kelley, Daniel Reines.

Writing – review & editing: Travis J. Loya, Thomas W. O’Rourke, William C. Simke, Joshua B. Kelley, Daniel Reines.

The authors thank Drs. Susan Wente (Vanderbilt University) and Anita Corbett (Emory University) for yeast strains and Dr. Graeme Conn for a critical reading of the manuscript.

We thank Laura Fox-Goharioon for assistance with microscopy.

The authors have declared that no competing interests exist.

Subjects:

Research Funding:

Research reported in this publication was supported by the National Institute of General Medical Sciences of the National Institutes of Health under award number [R01GM120271] to D. R. and R15 [GM128026] to J.K.

The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.

Keywords:

  • Science & Technology
  • Multidisciplinary Sciences
  • Science & Technology - Other Topics
  • RNA-BINDING PROTEINS
  • CELL-FREE FORMATION
  • TRANSCRIPTION TERMINATION
  • POLYMERASE-II
  • IMD2 TRANSCRIPTION
  • GENE-EXPRESSION
  • YEAST
  • NRD1
  • TRANSFORMATION
  • NUCLEOPORINS

Nab3 ' s localization to a nuclear granule in response to nutrient deprivation is determined by its essential prion-like domain

Journal Title:

PLoS ONE

Volume:

Volume 13, Number 12

Publisher:

, Pages e0209195-e0209195

Type of Work:

Article | Final Publisher PDF

Abstract:

Ribonucleoprotein (RNP) granules are higher order assemblies of RNA, RNA-binding proteins, and other proteins, that regulate the transcriptome and protect RNAs from environmental challenge. There is a diverse range of RNP granules, many cytoplasmic, which provide various levels of regulation of RNA metabolism. Here we present evidence that the yeast transcription termination factor, Nab3, is targeted to intranuclear granules in response to glucose starvation by Nab3's proline/glutamine-rich, prion-like domain (PrLD) which can assemble into amyloid in vitro. Localization to the granule is reversible and sensitive to the chemical probe 1,6 hexanediol suggesting condensation is driven by phase separation. Nab3's RNA recognition motif is also required for localization as seen for other PrLD-containing RNA-binding proteins that phase separate. Although the PrLD is necessary, it is not sufficient to localize to the granule. A heterologous PrLD that functionally replaces Nab3's essential PrLD, directed localization to the nuclear granule, however a chimeric Nab3 molecule with a heterologous PrLD that cannot restore termination function or viability, does not form granules. The Nab3 nuclear granule shows properties similar to well characterized cytoplasmic compartments formed by phase separation, suggesting that, as seen for other elements of the transcription machinery, termination factor condensation is functionally important.

Copyright information:

© 2018 Loya et al

This is an Open Access work distributed under the terms of the Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/).
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